Towards Non-stick Silk: Tuning the Hydrophobicity of Silk Fibroin Protein.

Autor: Fountain JN; Department of Chemistry, Tufts University, Medford, MA 02155, USA., Hawker MJ; Department of Chemistry and Biochemistry, California State University Fresno, Fresno, CA 93740, USA.; Department of Biomedical Engineering, Tufts University, Medford, MA 02155, USA., Hartle L; Department of Chemistry, Tufts University, Medford, MA 02155, USA.; Prime Impact Fund, Cambridge, MA 02139, USA., Wu J; Department of Biomedical Engineering, Tufts University, Medford, MA 02155, USA., Montanari V; Department of Chemistry, Tufts University, Medford, MA 02155, USA., Sahoo JK; Department of Biomedical Engineering, Tufts University, Medford, MA 02155, USA., Davis LM; Department of Chemistry, Tufts University, Medford, MA 02155, USA., Kaplan DL; Department of Biomedical Engineering, Tufts University, Medford, MA 02155, USA., Kumar K; Department of Chemistry, Tufts University, Medford, MA 02155, USA.; Department of Biomedical Engineering, Tufts University, Medford, MA 02155, USA.
Jazyk: angličtina
Zdroj: Chembiochem : a European journal of chemical biology [Chembiochem] 2022 Nov 18; Vol. 23 (22), pp. e202200429. Date of Electronic Publication: 2022 Sep 22.
DOI: 10.1002/cbic.202200429
Abstrakt: Silk fibroin protein is a biomaterial with excellent biocompatibility and low immunogenicity. These properties have catapulted the material as a leader for extensive use in stents, catheters, and wound dressings. Modulation of hydrophobicity of silk fibroin protein to further expand the scope and utility however has been elusive. We report that installing perfluorocarbon chains on the surface of silk fibroin transforms this water-soluble protein into a remarkably hydrophobic polymer that can be solvent-cast. A clear relationship emerged between fluorine content of the modified silk and film hydrophobicity. Water contact angles of the most decorated silk fibroin protein exceeded that of Teflon®. We further show that water uptake in prefabricated silk bars is dramatically reduced, extending their lifetimes, and maintaining mechanical integrity. These results highlight the power of chemistry under moderate conditions to install unnatural groups onto the silk fibroin surface and will enable further exploration into applications of this versatile biomaterial.
(© 2022 Wiley-VCH GmbH.)
Databáze: MEDLINE
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